clotting

This enzyme is closely associated with an endotoxin-sensitive hemolymph coagulation system which may play important roles in both hemostasis and host defense mechanisms. Its active form catalyzes the activation of clotting factor B. Clotting factor C Protein, Tachypleus tridentatus, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 33.8 kDa and the accession number is P28175.

This enzyme is closely associated with an endotoxin-sensitive hemolymph coagulation system which may play important roles in both hemostasis and host defense mechanisms. Its active form catalyzes the activation of factor B. Limulus clotting factor C Protein, Carcinoscorpius rotundicauda, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 42.2 kDa and the accession number is Q26422.

Thrombin-like snake venom serine protease that clots fibrinogen by releasing fibrinopeptide A from the alpha chain of fibrinogen (FGA), induces platelet aggregation through its interaction with GPIb (GP1BA GP1BB), and activates factor VIII (F8). SVTLE Protein, Bothrops jararaca, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 33.0 kDa and the accession number is P81661.

SVTLE Protein, Protobothrops flavoviridis, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 33.1 kDa and the accession number is P05620.

SVTLE Protein, Calloselasma rhodostoma, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 28.6 kDa and the accession number is P26324.

Thrombin-like snake venom serine protease that cleaves beta chain of fibrinogen (FGB), releasing fibrinopeptide B. Has a coagulant activity activating blood coagulation factors V (F5) and XIII (F13A1). Thrombin-like enzyme contortrixobin Protein, Agkistrodon contortrix, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 32.4 kDa and the accession number is P82981.

Thrombin-like snake venom serine protease. Has a coagulant activity. Acts on alpha-chains of fibrinogen (FGA) generating fibrinopeptide A. SVTLE Protein, Gloydius ussuriensis, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 33.7 kDa and the accession number is Q91053.

Mouse coagulation factor X F10 a member of the peptidase S1 family. The mature F10 is composed mostly of two EGF-like domains, one Gla gamma-carboxy-glutamate domain and one peptidase S1 domain. Factor Xa is a vitamin K-dependent plasma protease that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting. The two chains of F10 are formed from a single-chain precursor by the excision of two Arg residues. A single-chain precursor is initially synthesized in the liver. The light and heavy chains are linked together by disulfide bonds. The light chain contains a Gla and two EGF-like domains. The heavy chain corresponds to the serine protease domain. It can form a heterodimer with SERPINA5.

Kininogen-1 is a secreted protein which contains three cystatin domains. There are two alternatively spliced forms, designated as the high molecular weight (HMW) and low MW (LMW) forms. Kininogen-1 plays a critical role in blood coagulation and inflammatory response. Kininogens are inhibitors of thiol proteases. Kininogen-1 participates in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII, also inhibits the thrombin- and plasmin-induced aggregation of thrombocytes. The active peptide bradykinin that is released from Kininogen-1 shows a variety of physiological effects: influence in smooth muscle contraction, induction of hypotension, natriuresis and diuresis, decrease in blood glucose level. It is a mediator of inflammation and causes increase in vascular permeability, stimulation of nociceptors release of other mediators of inflammation. It has a cardioprotective effect. LMW-kininogen inhibits the aggregation of thrombocytes and doesn’t involved in blood clotting.

As protease inhibitors, serpins have an array of functions including regulating blood clotting, the complement pathway, extracellular matrix remodeling, and cell motility. Serpin G1 is a serine protease inhibitor protein. It is the largest member among the serpin class of proteins. Remarkably, Serpin G1 has a 2-domain structure, unlike most family members. The C-terminal serpin domain is similar to other serpins, and this part of Serpin G1 provides the inhibitory activity. The N-terminal domain is not essential for Serpin G1 to inhibit proteinases and has no similarity to other proteins. The main function of Serpin G1 is the inhibition of the complement system to prevent spontaneous activation. Serpin G1 is an acute phase protein and circulates in blood at levels of around 0.25g L, whose levels rise 2-fold during inflammation. Although named after its complement inhibitory activity, Serpin G1 also inhibits proteinases of the fibrinolytic, clotting, and kinin pathways. Most notably, Serpin G1 play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. It is also the most important physiological inhibitor of fXIIa, chymotrypsin and plasma kallikrein.

Fibrinogen-like protein 1 (FGL-1) is a protein that is structurally related to fibrinogen. In humans, FLG-1 is encoded by the FGL1 gene.Fibrinogen-like protein 1 is a member of the fibrinogen family of proteins, which also includes fibrinogen, fibrinogen-like protein 2, and clotting factors V, VIII, and XIII.Fibrinogen-like Protein 1 is a major immune inhibitory ligand of LAG-3.

Coagulation factor X, also known as FX, F10, Eponym Stuart-Prower factor, and thrombokinase, is an enzyme of the coagulation cascade. It is one of the vitamin K-dependent serine proteases, and plays a crucial role in the coagulation cascade and blood clotting, as the first enzyme in the common pathway of thrombus formation. Factor X deficiency is one of the rarest of the inherited coagulation disorders. FX deficiency among the most severe of the rare coagulation defects, typically including hemarthroses, hematomas, and umbilical cord, gastrointestinal, and central nervous system bleeding. Factor X is synthesized in the liver as a mature heterodimer formed from a single-chain precursor, and vitamin K is essential for its synthesis. Factor X is activated into factor Xa (FXa) by both factor IX (with its cofactor, factor VIII in a complex known as intrinsic Xase) and factor VII (with its cofactor, tissue factor in a complex known as extrinsic Xase) through cleaving the activation propeptide. As the first member of the final common pathway or thrombin pathway, FXa converts prothrombin to thrombin in the presence of factor Va, Ca2+, and phospholipid during blood clotting and cleaves prothrombin in two places (an arg-thr and then an arg-ile bond). This process is optimized when factor Xa is complexed with activated cofactor V in the prothrombinase complex. Inborn deficiency of factor X is very uncommon, and may present with epistaxis (nose bleeds), hemarthrosis (bleeding into joints) and gastrointestinal blood loss. Apart from congenital deficiency, low factor X levels may occur occasionally in a number of disease states. Furthermore, factor X deficiency may be seen in amyloidosis, where factor X is adsorbed to the amyloid fibrils in the vasculature.

F10, also known as Coagulation factor X, belongs to the peptidase S1 family that is synthesized as a 488 amino acid (aa) with a signal peptide and a pro region (residues 1‑40). Both the intrinsic and extrinsic pathways activate Factor X to Xa, which consists of light (residues 41‑179) and heavy (residues 235‑488) chains linked by a disulfide bond. Coagulation factor X is initially synthesized in the liver. The two chains are formed from a single-chain precursor by the excision of two Arg residues and are held together by 1 or more disulfide bonds. Forms a heterodimer with SERPINA5. F10 is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.